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Characterization of a bovine mammary gland PP3 cDNA reveals homology with mouse and rat adhesion molecule GlyCAM-1.
Johnsen, L B; Sørensen, E S; Petersen, T E; Berglund, L.
Afiliação
  • Johnsen LB; Protein Chemistry Laboratory, University of Aarhus, Denmark.
Biochim Biophys Acta ; 1260(1): 116-8, 1995 Jan 02.
Article em En | MEDLINE | ID: mdl-7999787
ABSTRACT
A full length PP3 (Proteose-Peptone component 3) cDNA of 679 bp was isolated from a bovine mammary gland cDNA library. The cDNA encodes a signal peptide of 18 amino acids followed by the mature PP3 sequence of 135 amino acids. This polypeptide showed homology with mouse and rat GlyCAM-1 (Glycosylation dependent Cell Adhesion Molecule 1) a protein which has been shown to act as a ligand for lymphocytes. The similarity was most profound between the signal peptides and three short regions of the mature polypeptides. Additionally structural conservation was predicted by computer analysis in the shape of a C-terminal amphipathic helix. PP3 was found to be expressed in mammary gland but not in peripheral lymph nodes, Peyer's pathes, lung, spleen, heart, and muscle.
Assuntos
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Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Glicoproteínas / Caseínas / Glândulas Mamárias Animais / Mucinas Limite: Animals Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Dinamarca
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Base de dados: MEDLINE Assunto principal: Fragmentos de Peptídeos / Glicoproteínas / Caseínas / Glândulas Mamárias Animais / Mucinas Limite: Animals Idioma: En Revista: Biochim Biophys Acta Ano de publicação: 1995 Tipo de documento: Article País de afiliação: Dinamarca